Interleukin 1 and tumor necrosis factor stimulate two novel protein kinases that phosphorylate the heat shock protein hsp27 and beta-casein.

Guesdon, François; Freshney, Norman W.; Waller, R J; Rawlinson, Lesley; Saklatvala, Jeremy

doi:10.1016/s0021-9258(18)53601-2

Cited by 121 publications

(24 citation statements)

References 45 publications

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“…The p54 and p38 MAP kinases on the other hand are strongly activated by stresses and cytokines, but only weakly by mitogens or phorbol ester. One cytosolic kinase has been found which appears to be quite specifically activated by IL1 and TN F (Guesdon et al 1993(Guesdon et al , 1994. This enzyme phosphorylates vitro the milk protein, /Lcasein on S eri42 (F. Guesdon, unpublished data).…”

Section: ( G) /} Casein Kinasementioning

confidence: 99%

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Interleukin 1 (IL1) and tumour necrosis factor (TNF) signal transduction

Saklatvala

Davis

Guesdon

1996

Phil. Trans. R. Soc. Lond. B

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The inflammatory cytokines interleukin 1 (IL1) and tumour necrosis factor (TNF) have a broad range of physiological effects. Whereas their immediate post-receptor events are not well understood, both have the potential to activate a range of protein kinases. These include the three types of mitogen activated protein (MAP) kinase (ERK, JNK/p54 and p38) and a beta-casein kinase. The mechanisms by which these kinases are activated is discussed and the significance of their activation for particular biological responses is assessed.

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Section: ( G) /} Casein Kinasementioning

confidence: 99%

“…IL1 and TN F activate p42 and p44 MAP kinases (also called ER K for extracellular signal regulated kinases) in a variety of cultured connective tissue cells, such as fibroblasts, vascular endothelial cells and chondrocytes (Guy et al 1991;Guesdon at. 1993).…”

Section: (B) P42 and P44 M Ap Kinases ( And 1)mentioning

confidence: 99%

Interleukin 1 (IL1) and tumour necrosis factor (TNF) signal transduction

Saklatvala

Davis

Guesdon

1996

Phil. Trans. R. Soc. Lond. B

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“…TNF is an inflammatory cytokine whose spectrum of action, effects, and signal transduction pathways are remarkably similar to those of IL-1 (28)(29)(30)(31). Ceils transfected with IL-1 RII retained responsiveness to TNF.…”

Section: Inhibition Of Ll-i Responsiveness Bymentioning

confidence: 99%

Inhibition of interleukin-1 responsiveness by type II receptor gene transfer: a surface "receptor" with anti-interleukin-1 function.

Sironi

Muzio

et al. 1996

The Journal of Experimental Medicine

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SummaryThe hypothesis that the type II receptor (RII) acts as a decoy for interleukin-1 (IL-1) was tested by gene transfer in cells expressing only the type I receptor (8387 fibroblasts). RII-transfected cells showed defective responsiveness to IL-1 in terms of NFkB activation, cytokine gene expression and production. Blocking monoclonal antibodies against RII restored the capacity of RII-transfected cells to respond to IL-113. Hence defective IL-1 responsiveness of RlI-transfected cells requires surface expression of the molecule. RII-transfected cells showed normal responsiveness to TNF, which shares functional properties and elements in the signal transduction pathway with IL-1. Cells transfected with a deletion mutant of RII missing 26 of 29 amino acids of the cytoplasmic portion of the molecule showed impaired responsiveness to IL-1. Cells transfected with the full-length or the cytoplasmic deletion mutant of RII released copious amounts of RII in the supernatant. However, transfected cells showed defective responsiveness to brief exposure to IL-1, in the absence of measurable released RII. These results indicate that impairment of the responsiveness to IL-1 following RII gene transfer was dependent upon surface expression of the molecule, specific for IL-1 and unaffected by truncation of the cytoplasmic portion. Thus, the type II "receptor" is a decoy surface molecule, regulated by antiinflammatory signals, whose only known function is to capture and block IL-1.

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“…T669 peptide is a substrate for p42/p44 MAP kinase, which IL-1 activates strongly in some cultured ceils (4)(5)(6). We were surprised that essentially all the enzyme we detected could be accounted for by p50 and p55 and there was little evidence of any activated enzyme corresponding to p42/p44 MAP kinase.…”

Section: Discussionmentioning

confidence: 68%

“…Some of the enzymes involved have been identified. For example, components of the growth factorregulated pathway, the p42/p44 mitogen-activated protein (MAP) 1 kinases and their activator, MAP kinase kinase, are stimulated in some cdls (4)(5)(6).…”

mentioning

confidence: 99%

Interleukin 1 alpha activates two forms of p54 alpha mitogen-activated protein kinase in rabbit liver.

Kracht

Truong

Totty

et al. 1994

The Journal of Experimental Medicine

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SummaryWe have identified in rabbits two hepatic forms of T669 peptide kinases that are very strongly activated after systemic injection with the inflammatory cytokiue interleukin 1 (ID1). The T669 peptide contains a major phosphoryhtion site of the epidermal growth factor receptor, threonine 699 and is a substrate for mitogen-activated protein (MAP) kinases. The kinases were purified to homogeneity and corresponded to 50-and 55-kD proteins on sodium dodecyl sulfate-polyaerylamide gel electrophoresis. Amino add sequencing of 12 tryptic peptides of both kinases identified them as p54 MAP kinase or. This kinase belongs to the novel family of stress-activated protein kinag's. This is the first evidence of IL-1 activating a spedfic protein kinase in vivo.

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Interleukin 1 and tumor necrosis factor stimulate two novel protein kinases that phosphorylate the heat shock protein hsp27 and beta-casein.

Cited by 121 publications

References 45 publications

Interleukin 1 (IL1) and tumour necrosis factor (TNF) signal transduction

Interleukin 1 (IL1) and tumour necrosis factor (TNF) signal transduction

Inhibition of interleukin-1 responsiveness by type II receptor gene transfer: a surface "receptor" with anti-interleukin-1 function.

Interleukin 1 alpha activates two forms of p54 alpha mitogen-activated protein kinase in rabbit liver.

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